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Murein (peptidoglycan) structure, architecture and biosynthesis in Escherichia coli

Lookup NU author(s): Professor Waldemar Vollmer


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The periplasmic murein (peptidoglycan) sacculus is a giant macromolecule made of glycan strands cross-linked by short peptides completely surrounding the cytoplasmic membrane to protect the cell from lysis due to its internal osmotic pressure. More than 50 different muropeptides are released from the sacculus by treatment with a muramidase. Escherichia coli has six murein synthases which enlarge the sacculus by transglycosylation and transpeptidation of lipid II precursor. A set of twelve periplasmic murein hydrolases (autolysins) release murein fragments during cell growth and division. Recent data on the in vitro murein synthesis activities of the murein synthases and on the interactions between murein synthases, hydrolases and cell cycle related proteins are being summarized. There are different models for the architecture of murein and for the incorporation of new precursor into the sacculus. We present a model in which morphogenesis of the rod-shaped E. coli is driven by cytoskeleton elements competing for the control over the murein synthesis multi-enzyme complexes. © 2007 Elsevier B.V. All rights reserved.

Publication metadata

Author(s): Vollmer W, Bertsche U

Publication type: Article

Publication status: Published

Journal: Biochimica et Biophysica Acta - Biomembranes

Year: 2008

Volume: 1778

Issue: 9

Pages: 1714-1734

ISSN (print): 0005-2736

Publisher: Elsevier


DOI: 10.1016/j.bbamem.2007.06.007


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Funder referenceFunder name
Deutsche Forschungsgemeinschaft (DFG)
FOR 449Forschergruppe Bakterielle Zellhulle
LSHM-CT-2004-512138European Commission